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Items: 1 to 20 of 34


Computational Studies on Water-Catalyzed Mechanisms for Stereoinversion of Glutarimide Intermediates Formed from Glutamic Acid Residues in Aqueous Phase.

Nakayoshi T, Fukuyoshi S, Kato K, Kurimoto E, Oda A.

Int J Mol Sci. 2019 May 15;20(10). pii: E2410. doi: 10.3390/ijms20102410.


Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits.

Sekiguchi T, Satoh T, Kurimoto E, Song C, Kozai T, Watanabe H, Ishii K, Yagi H, Yanaka S, Uchiyama S, Uchihashi T, Murata K, Kato K.

Int J Mol Sci. 2019 May 9;20(9). pii: E2308. doi: 10.3390/ijms20092308.


Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer.

Satoh T, Yagi-Utsumi M, Okamoto K, Kurimoto E, Tanaka K, Kato K.

Int J Mol Sci. 2019 May 7;20(9). pii: E2231. doi: 10.3390/ijms20092231.


Possible Mechanisms of Nonenzymatic Formation of Dehydroalanine Residue Catalyzed by Dihydrogen Phosphate Ion.

Nakayoshi T, Kato K, Kurimoto E, Oda A.

J Phys Chem B. 2019 Apr 18;123(15):3147-3155. doi: 10.1021/acs.jpcb.8b10386. Epub 2019 Apr 9.


Computational studies on the water-catalyzed stereoinversion mechanism of glutamic acid residues in peptides and proteins.

Nakayoshi T, Kato K, Fukuyoshi S, Takahashi O, Kurimoto E, Oda A.

Chirality. 2018 May;30(5):527-535. doi: 10.1002/chir.22841. Epub 2018 Mar 12.


Validation of molecular force field parameters for peptides including isomerized amino acids.

Oda A, Nakayoshi T, Fukuyoshi S, Kurimoto E, Yamaotsu N, Hirono S, Takahashi O.

Chirality. 2018 Apr;30(4):332-341. doi: 10.1002/chir.22821. Epub 2018 Feb 2.


The assembly mechanism of coiled-coil domains of the yeast cargo receptors Emp46p/47p and the mutational alteration of pH-dependency of complex formation.

Kato K, Furuhashi T, Kato K, Oda A, Kurimoto E.

J Biochem. 2018 May 1;163(5):441-446. doi: 10.1093/jb/mvy011.


Influences of conformations of peptides on stereoinversions and/or isomerizations of aspartic acid residues.

Oda A, Nakayoshi T, Fukuyoshi S, Kurimoto E, Takahashi O.

Biochim Biophys Acta Proteins Proteom. 2018 Jul;1866(7):783-788. doi: 10.1016/j.bbapap.2018.01.006. Epub 2018 Jan 11.


Comparison of the activation energy barrier for succinimide formation from α- and β-aspartic acid residues obtained from density functional theory calculations.

Nakayoshi T, Kato K, Fukuyoshi S, Takahashi O, Kurimoto E, Oda A.

Biochim Biophys Acta Proteins Proteom. 2018 Jul;1866(7):759-766. doi: 10.1016/j.bbapap.2017.12.011. Epub 2018 Jan 3.


Validation of Molecular Dynamics Simulations for Prediction of Three-Dimensional Structures of Small Proteins.

Kato K, Nakayoshi T, Fukuyoshi S, Kurimoto E, Oda A.

Molecules. 2017 Oct 12;22(10). pii: E1716. doi: 10.3390/molecules22101716.


Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation.

Kurimoto E, Satoh T, Ito Y, Ishihara E, Okamoto K, Yagi-Utsumi M, Tanaka K, Kato K.

Protein Sci. 2017 May;26(5):1080-1085. doi: 10.1002/pro.3153. Epub 2017 Mar 16.


pH-Dependent Assembly and Segregation of the Coiled-Coil Segments of Yeast Putative Cargo Receptors Emp46p and Emp47p.

Ishii K, Enda H, Noda M, Kajino M, Kim A, Kurimoto E, Sato K, Nakano A, Kobayashi Y, Yagi H, Uchiyama S, Kato K.

PLoS One. 2015 Oct 8;10(10):e0140287. doi: 10.1371/journal.pone.0140287. eCollection 2015.


Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinase activity.

Satoh T, Sumiyoshi A, Yagi-Utsumi M, Sakata E, Sasakawa H, Kurimoto E, Yamaguchi Y, Li W, Joazeiro CA, Hirokawa T, Kato K.

FEBS Lett. 2014 Nov 28;588(23):4422-30. doi: 10.1016/j.febslet.2014.10.013. Epub 2014 Oct 19.


Structural and functional mosaic nature of MHC class I molecules in their peptide-free form.

Kurimoto E, Kuroki K, Yamaguchi Y, Yagi-Utsumi M, Igaki T, Iguchi T, Maenaka K, Kato K.

Mol Immunol. 2013 Oct;55(3-4):393-9. doi: 10.1016/j.molimm.2013.03.014. Epub 2013 Apr 8.


Spatial arrangement and functional role of α subunits of proteasome activator PA28 in hetero-oligomeric form.

Sugiyama M, Sahashi H, Kurimoto E, Takata S, Yagi H, Kanai K, Sakata E, Minami Y, Tanaka K, Kato K.

Biochem Biophys Res Commun. 2013 Mar 1;432(1):141-5. doi: 10.1016/j.bbrc.2013.01.071. Epub 2013 Jan 29.


NMR and mutational identification of the collagen-binding site of the chaperone Hsp47.

Yagi-Utsumi M, Yoshikawa S, Yamaguchi Y, Nishi Y, Kurimoto E, Ishida Y, Homma T, Hoseki J, Nishikawa Y, Koide T, Nagata K, Kato K.

PLoS One. 2012;7(9):e45930. doi: 10.1371/journal.pone.0045930. Epub 2012 Sep 25.


A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex.

Yagi H, Ishimoto K, Hiromoto T, Fujita H, Mizushima T, Uekusa Y, Yagi-Utsumi M, Kurimoto E, Noda M, Uchiyama S, Tokunaga F, Iwai K, Kato K.

EMBO Rep. 2012 May 1;13(5):462-8. doi: 10.1038/embor.2012.24.


Backbone and side chain 1H, 13C, and 15N assignments of the ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex.

Uekusa Y, Mimura S, Sasakawa H, Kurimoto E, Sakata E, Olivier S, Yagi H, Tokunaga F, Iwai K, Kato K.

Biomol NMR Assign. 2012 Oct;6(2):177-80. doi: 10.1007/s12104-011-9350-1. Epub 2011 Nov 30.


Kinetic asymmetry of subunit exchange of homooligomeric protein as revealed by deuteration-assisted small-angle neutron scattering.

Sugiyama M, Kurimoto E, Yagi H, Mori K, Fukunaga T, Hirai M, Zaccai G, Kato K.

Biophys J. 2011 Oct 19;101(8):2037-42. doi: 10.1016/j.bpj.2011.09.004.


Functional characterization of human cyclin T1 N-terminal region for human immunodeficiency virus-1 Tat transcriptional activation.

Asamitsu K, Hibi Y, Imai K, Victoriano AF, Kurimoto E, Kato K, Okamoto T.

J Mol Biol. 2011 Jul 29;410(5):887-95. doi: 10.1016/j.jmb.2011.04.061.


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